Cloning, nucleotide sequence and amplified expression of the gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G.
The gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G has been cloned in Escherichia coli DH5 alpha MCR via pBR322 or 325, and then transferred into Streptomyces lividans TK24 via pIJ486, with substantial amplification of the expressed DD-peptidase. The gene has the information for the synthesis of a 255 amino acid precursor, the amino terminal region of which has the characteristic features of a signal peptide. The primary structure as deduced from nucleotide sequencing confirms that previously determined by chemical methods except for the occurrence of an Asp instead of Asn at position 1 and an additional Ala immediately downstream of Pro67.
Duez
C
C
Service de Microbiologie, Université de Liège, Sart Tilman, Belgium.
Lakaye
B
B
Houba
S
S
Dusart
J
J
Ghuysen
J M
JM
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004792:Enzyme Precursors / Q000096:biosynthesis / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D021382:Protein Sorting Signals / Q000235:genetics; D013302:Streptomyces / Q000201:enzymology / Q000235:genetics*
D004792:Enzyme Precursors; D021382:Protein Sorting Signals; D002267:Muramoylpentapeptide Carboxypeptidase